33f186d15be5bc81770f85b829a26336 catalysts_a2020v10n11p1277.pdf 84b9b63318417e44c5cde724fba627594c745ec5 catalysts_a2020v10n11p1277.pdf b9e985ebb3d98ebe4713d45a97cb529098e14f9d28c5f8d96c2182b83f475cf1 catalysts_a2020v10n11p1277.pdf Title: Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications Subject: Lipases are biocatalysts with a significant potential to enable a shift from current pollutant manufacturing processes to environmentally sustainable approaches. The main reason of this prospect is their catalytic versatility as they carry out several industrially relevant reactions as hydrolysis of fats in water/lipid interface and synthesis reactions in solvent-free or non-aqueous media such as transesterification, interesterification and esterification. Because of the outstanding traits of Rhizopus oryzae lipase (ROL), 1,3-specificity, high enantioselectivity and stability in organic media, its application in energy, food and pharmaceutical industrial sector has been widely studied. Significant advances have been made in the biochemical characterisation of ROL particularly in how its activity and stability are affected by the presence of its prosequence. In addition, native and heterologous production of ROL, the latter in cell factories like Escherichia coli, Saccharomyces cerevisiae and Komagataella phaffii (Pichia pastoris), have been thoroughly described. Therefore, in this review, we summarise the current knowledge about R. oryzae lipase (i) biochemical characteristics, (ii) production strategies and (iii) potential industrial applications. Keywords: Rhizopus oryzae lipase; Pichia pastoris; biodiesel; structured lipids; flavour; ester; bioprocess engineering; operational strategy; racemic resolution Author: Josu López-Fernández, M. Dolors Benaiges and Francisco Valero Creator: LaTeX with hyperref package Producer: pdfTeX-1.40.18 CreationDate: Thu Nov 5 09:58:07 2020 CET ModDate: Thu Nov 5 10:11:01 2020 CET Custom Metadata: no Metadata Stream: no Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 50 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 2486350 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- WPKMNW+URWPalladioL-Ital Type 1 Custom yes yes no 10 0 XWYBBW+Rpxi Type 1 Builtin yes yes no 15 0 ENBEKA+URWPalladioL-BoldItal Type 1 Custom yes yes no 19 0 NVBPTD+URWPalladioL-Bold Type 1 Custom yes yes no 23 0 TGOSIS+URWPalladioL-Roma Type 1 Custom yes yes no 27 0 DXFCOI+Rpxr Type 1 Builtin yes yes no 31 0 ENXZUH+VnURWPalladioL-Bold Type 1 Custom yes yes no 35 0 DIQUYV+VnURWPalladioL Type 1 Custom yes yes no 40 0 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PDFMetadata: Objects: 1466 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: section.1 Item: Title: Biochemical Properties Destination: section.2 Item: Title: Rhizopus oryzae Lipase Production and Bioprocess Engineering Destination: section.3 Children: Item: Title: Komogatella Phaffii Cell Factory Destination: subsection.3.1 Children: Item: Title: rROL PAOX Destination: subsubsection.3.1.1 Item: Title: rROL PFLD1 Destination: subsubsection.3.1.2 Item: Title: proROL PAOX Destination: subsubsection.3.1.3 Item: Title: rROL and proROL PGAP Destination: subsubsection.3.1.4 Item: Title: 28proROL PAOX Destination: subsubsection.3.1.5 Item: Title: Whole Cells Destination: subsubsection.3.1.6 Item: Title: Industrial Applications of Rhizopus oryzae Lipase Destination: section.4 Children: Item: Title: Biodiesel Production Destination: subsection.4.1 Item: Title: Structured Lipids Production Destination: subsection.4.2 Item: Title: Flavour Esters Production Destination: subsection.4.3 Item: Title: Resolution of Racemic Mixtures Destination: subsection.4.4 Item: Title: References Destination: figure.caption.19 Info: Title: Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications Author: Josu López-Fernández, M. Dolors Benaiges and Francisco Valero Subject: Lipases are biocatalysts with a significant potential to enable a shift from current pollutant manufacturing processes to environmentally sustainable approaches. The main reason of this prospect is their catalytic versatility as they carry out several industrially relevant reactions as hydrolysis of fats in water/lipid interface and synthesis reactions in solvent-free or non-aqueous media such as transesterification, interesterification and esterification. Because of the outstanding traits of Rhizopus oryzae lipase (ROL), 1,3-specificity, high enantioselectivity and stability in organic media, its application in energy, food and pharmaceutical industrial sector has been widely studied. Significant advances have been made in the biochemical characterisation of ROL particularly in how its activity and stability are affected by the presence of its prosequence. In addition, native and heterologous production of ROL, the latter in cell factories like Escherichia coli, Saccharomyces cerevisiae and Komagataella phaffii (Pichia pastoris), have been thoroughly described. Therefore, in this review, we summarise the current knowledge about R. oryzae lipase (i) biochemical characteristics, (ii) production strategies and (iii) potential industrial applications. 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319, 198, 357, 209 Annotation: Subtype: Link Rect: 415, 172, 453, 183 Annotation: Subtype: Link Rect: 315, 133, 353, 144 Annotation: Subtype: Link Rect: 366, 107, 403, 118 Annotation: Subtype: Link Rect: 387, 82, 424, 92 Page: Sequence: 50 Annotations: Annotation: Subtype: Link Rect: 150, 689, 187, 699 Annotation: Subtype: Link Rect: 272, 663, 309, 673 Annotation: Subtype: Link Rect: 219, 624, 256, 635 Annotation: Subtype: Link Rect: 168, 586, 205, 596 Annotation: Subtype: Link Rect: 295, 560, 333, 570 Annotation: Subtype: Link Rect: 459, 521, 496, 531 Annotation: Subtype: Link Rect: 246, 483, 283, 493 Annotation: Subtype: Link Rect: 362, 456, 399, 467 Annotation: Subtype: Link Rect: 456, 430, 493, 441 Annotation: Subtype: Link Rect: 393, 404, 431, 415 Annotation: Subtype: Link Rect: 308, 366, 345, 376 Annotation: Subtype: Link Rect: 76, 294, 166, 325 Annotation: Subtype: Link Rect: 234, 288, 407, 299 Checksum: 89c7a3f8 Type: CRC32 Checksum: 33f186d15be5bc81770f85b829a26336 Type: MD5 Checksum: 84b9b63318417e44c5cde724fba627594c745ec5 Type: SHA-1 Checksum: b9e985ebb3d98ebe4713d45a97cb529098e14f9d28c5f8d96c2182b83f475cf1 Type: SHA-256